Header list of 1l3n.pdb file
Complete list - ct 27 Bytes
HEADER OXIDOREDUCTASE 28-FEB-02 1L3N
TITLE THE SOLUTION STRUCTURE OF REDUCED DIMERIC COPPER ZINC SOD: THE
TITLE 2 STRUCTURAL EFFECTS OF DIMERIZATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: SOD;
COMPND 5 EC: 1.15.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SOD1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TOPP1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBR322
KEYWDS REDUCED HUMAN COPPER/ZINC SUPEROXIDE DISMUTASE, SOLUTION STRUCTURE,
KEYWDS 2 HOMODIMERIC PROTEIN., OXIDOREDUCTASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR L.BANCI,I.BERTINI,F.CRAMARO,R.DEL CONTE,M.S.VIEZZOLI
REVDAT 4 27-OCT-21 1L3N 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1L3N 1 VERSN
REVDAT 2 01-APR-03 1L3N 1 JRNL
REVDAT 1 08-MAY-02 1L3N 0
JRNL AUTH L.BANCI,I.BERTINI,F.CRAMARO,R.DEL CONTE,M.S.VIEZZOLI
JRNL TITL THE SOLUTION STRUCTURE OF REDUCED DIMERIC COPPER ZINC
JRNL TITL 2 SUPEROXIDE DISMUTASE. THE STRUCTURAL EFFECTS OF DIMERIZATION
JRNL REF EUR.J.BIOCHEM. V. 269 1905 2002
JRNL REFN ISSN 0014-2956
JRNL PMID 11952792
JRNL DOI 10.1046/J.1432-1033.2002.02840.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.BANCI,I.BERTINI,F.CRAMARO,R.DEL CONTE,A.ROSATO,
REMARK 1 AUTH 2 M.S.VIEZZOLI
REMARK 1 TITL BACKBONE DYNAMICS OF HUMAN CU,ZN SUPEROXIDE DISMUTASE AND OF
REMARK 1 TITL 2 ITS MONOMERIC F50E/G51E/E133Q MUTANT: THE INFLUENCE OF
REMARK 1 TITL 3 DIMERIZATION ON MOBILITY AND FUNCTION
REMARK 1 REF BIOCHEMISTRY V. 39 9108 2000
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI000067Z
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CALIBA, AMBER
REMARK 3 AUTHORS : GUENTER ET AL. (CALIBA), PEARLMAN ET AL. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES WERE CALCULATED USING THE CONSTRAINTS: 3566 NOE
REMARK 3 CROSS PEAKS WERE CONVERTED INTO DISTANCE CONSTRAINTS, 49 DIHEDRAL
REMARK 3 PHI ANGLES, 52 DIHEDRAL PSI ANGLES, 14 CHI ANGLES AND 45 PROTON
REMARK 3 PAIRS STEREOSPECIFICALLY ASSIGNED.
REMARK 3 THE CU(I) AND ZN(II) METAL IONS WERE INCLUDED IN THE CALCULATION
REMARK 3 WITH SPECIAL LINKERS.
REMARK 3 THE DISULFIDE BRIDGE BETWEEN CYS57 AND CYS146 WAS INTRODUCED WITH
REMARK 3 UPPER AND LOWER DISTANCE LIMITS BETWEEN THE CB AND SG ATOMS OF THE
REMARK 3 TWO SIDE CHAINS.
REMARK 4
REMARK 4 1L3N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015613.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296; 286
REMARK 210 PH : 5.0; 5.0
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : CU(I),ZN(II) SOD 2MM ENRICHED IN
REMARK 210 15N; CU(I),ZN(II) SOD 2MM
REMARK 210 ENRICHED IN 15N, 13C; CU(I),
REMARK 210 ZN(II) SOD 2MM ENRICHED IN 15N,
REMARK 210 13C AND 2H AT 70%; CU(I),ZN(II)
REMARK 210 SOD 2MM ENRICHED IN 15N
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D HNCA, 3D NH(CO)CA, 3D HNCO,
REMARK 210 3D HN(CA)CO-TROSY LIKE, 2D 15N-
REMARK 210 HSQC, 2D 13C-HSQC, 3D 13C-NOESY-
REMARK 210 HSQC; 3D H(C)CH-TOCSY, 3D (H)CCH-
REMARK 210 TOCSY; 3D 15N-NOESY-HSQC, 3D
REMARK 210 HNHA, 3D HNHB, 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 700 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GLOMSA, DYANA, XWINNMR, PROCHECK
REMARK 210 -NMR
REMARK 210 METHOD USED : SIMULATED ANNEALING AND
REMARK 210 RESTRAINED ENEGY MINIMIZATION IN
REMARK 210 VACUUM
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURE WITH THE LOWEST ENERGY
REMARK 210 TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: CU(I), ZN(II) SOD STRUCTURE WAS DETERMINED USING TRIPLE
REMARK 210 RESONANCE THREE-AND BI-DIMENSIONAL AND HOMONUCLEAR BI-
REMARK 210 DIMENSIONAL TECHNIQUES.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 11 ARG A 143 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 11 ARG B 143 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 12 ARG B 143 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 14 CYS A 57 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 14 CYS A 146 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 14 ARG B 115 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 17 ARG B 69 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 17 ARG B 69 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 19 ARG A 115 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 24 ARG B 143 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 27 ARG B 143 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 28 ARG A 143 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 28 CYS B 146 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 29 ARG B 69 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 THR A 2 -41.08 -166.22
REMARK 500 1 VAL A 14 97.30 -63.94
REMARK 500 1 ILE A 17 83.69 -156.47
REMARK 500 1 VAL A 31 59.14 -97.31
REMARK 500 1 HIS A 48 161.96 57.10
REMARK 500 1 THR A 58 -54.61 -157.66
REMARK 500 1 ALA A 60 -38.47 -30.26
REMARK 500 1 PRO A 62 -167.13 -79.29
REMARK 500 1 SER A 68 100.85 -58.63
REMARK 500 1 ARG A 69 -90.47 -113.78
REMARK 500 1 PRO A 74 1.26 -68.83
REMARK 500 1 ARG A 79 138.46 -33.45
REMARK 500 1 VAL A 81 39.32 -72.85
REMARK 500 1 SER A 98 71.28 -154.52
REMARK 500 1 SER A 102 57.09 -110.96
REMARK 500 1 VAL A 103 -61.73 -141.77
REMARK 500 1 LYS A 136 -81.17 -118.60
REMARK 500 1 ASN A 139 36.87 178.71
REMARK 500 1 ILE A 149 -86.79 -76.66
REMARK 500 1 ILE A 151 152.64 63.80
REMARK 500 1 ASP B 52 124.00 -24.12
REMARK 500 1 ALA B 60 2.01 -51.35
REMARK 500 1 SER B 68 102.41 -58.39
REMARK 500 1 ARG B 69 -87.88 -132.48
REMARK 500 1 PRO B 74 10.12 -69.11
REMARK 500 1 VAL B 81 -69.76 -174.20
REMARK 500 1 SER B 98 57.40 -158.69
REMARK 500 1 VAL B 103 -51.99 -148.00
REMARK 500 1 LYS B 128 48.77 -82.21
REMARK 500 1 ASN B 139 17.35 56.09
REMARK 500 2 THR A 2 -23.95 125.01
REMARK 500 2 ASN A 53 15.60 -153.82
REMARK 500 2 CYS A 57 60.27 15.36
REMARK 500 2 THR A 58 -61.77 -132.18
REMARK 500 2 ARG A 69 -96.27 -122.92
REMARK 500 2 VAL A 81 -87.35 -160.48
REMARK 500 2 ASP A 90 172.09 -59.63
REMARK 500 2 SER A 98 58.85 -158.05
REMARK 500 2 SER A 107 -165.58 -120.10
REMARK 500 2 ASP A 109 -57.54 71.07
REMARK 500 2 SER A 111 85.05 39.84
REMARK 500 2 LYS A 136 -75.84 -111.50
REMARK 500 2 ARG A 143 68.01 -66.46
REMARK 500 2 ILE A 149 -87.70 -65.81
REMARK 500 2 THR B 2 -46.88 -166.38
REMARK 500 2 VAL B 14 99.74 -68.71
REMARK 500 2 GLN B 22 86.90 -158.84
REMARK 500 2 GLU B 49 -113.68 4.00
REMARK 500 2 PHE B 50 -141.88 -95.29
REMARK 500 2 ASN B 53 12.07 -163.45
REMARK 500
REMARK 500 THIS ENTRY HAS 1072 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 69 0.12 SIDE CHAIN
REMARK 500 1 PHE B 50 0.10 SIDE CHAIN
REMARK 500 1 PHE B 64 0.09 SIDE CHAIN
REMARK 500 2 PHE A 45 0.07 SIDE CHAIN
REMARK 500 2 ARG B 69 0.17 SIDE CHAIN
REMARK 500 2 ARG B 115 0.08 SIDE CHAIN
REMARK 500 3 PHE A 64 0.09 SIDE CHAIN
REMARK 500 3 ARG A 115 0.30 SIDE CHAIN
REMARK 500 3 PHE B 50 0.08 SIDE CHAIN
REMARK 500 3 PHE B 64 0.11 SIDE CHAIN
REMARK 500 3 ARG B 79 0.10 SIDE CHAIN
REMARK 500 4 ARG A 115 0.11 SIDE CHAIN
REMARK 500 4 PHE B 45 0.09 SIDE CHAIN
REMARK 500 4 PHE B 64 0.08 SIDE CHAIN
REMARK 500 4 HIS B 71 0.08 SIDE CHAIN
REMARK 500 5 ARG A 69 0.11 SIDE CHAIN
REMARK 500 5 ARG A 115 0.09 SIDE CHAIN
REMARK 500 5 PHE B 64 0.09 SIDE CHAIN
REMARK 500 6 ARG A 143 0.13 SIDE CHAIN
REMARK 500 6 HIS B 71 0.10 SIDE CHAIN
REMARK 500 7 PHE A 50 0.12 SIDE CHAIN
REMARK 500 7 PHE A 64 0.11 SIDE CHAIN
REMARK 500 7 ARG A 115 0.10 SIDE CHAIN
REMARK 500 7 PHE B 64 0.09 SIDE CHAIN
REMARK 500 7 ARG B 79 0.10 SIDE CHAIN
REMARK 500 8 PHE A 64 0.09 SIDE CHAIN
REMARK 500 8 ARG A 115 0.10 SIDE CHAIN
REMARK 500 8 ARG A 143 0.09 SIDE CHAIN
REMARK 500 8 ARG B 143 0.09 SIDE CHAIN
REMARK 500 9 HIS A 48 0.17 SIDE CHAIN
REMARK 500 9 ARG A 69 0.08 SIDE CHAIN
REMARK 500 9 ARG A 115 0.08 SIDE CHAIN
REMARK 500 9 ARG A 143 0.09 SIDE CHAIN
REMARK 500 9 ARG B 115 0.13 SIDE CHAIN
REMARK 500 9 ARG B 143 0.09 SIDE CHAIN
REMARK 500 10 HIS A 48 0.14 SIDE CHAIN
REMARK 500 10 ARG A 143 0.12 SIDE CHAIN
REMARK 500 11 PHE A 64 0.09 SIDE CHAIN
REMARK 500 11 PHE B 20 0.09 SIDE CHAIN
REMARK 500 11 PHE B 64 0.16 SIDE CHAIN
REMARK 500 11 ARG B 115 0.09 SIDE CHAIN
REMARK 500 12 ARG A 79 0.11 SIDE CHAIN
REMARK 500 12 ARG A 143 0.09 SIDE CHAIN
REMARK 500 12 HIS B 80 0.11 SIDE CHAIN
REMARK 500 13 PHE A 20 0.08 SIDE CHAIN
REMARK 500 13 PHE A 64 0.11 SIDE CHAIN
REMARK 500 13 ARG B 115 0.10 SIDE CHAIN
REMARK 500 14 ARG A 69 0.08 SIDE CHAIN
REMARK 500 14 PHE B 45 0.10 SIDE CHAIN
REMARK 500 14 HIS B 46 0.07 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 102 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 A 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 46 ND1
REMARK 620 2 HIS A 48 NE2 133.2
REMARK 620 3 HIS A 120 NE2 91.0 118.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 63 ND1
REMARK 620 2 HIS A 71 ND1 105.0
REMARK 620 3 HIS A 80 ND1 111.7 117.2
REMARK 620 4 ASP A 83 OD2 151.8 87.3 83.3
REMARK 620 5 ASP A 83 OD1 94.9 105.5 119.5 57.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 B 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 46 ND1
REMARK 620 2 HIS B 48 NE2 129.5
REMARK 620 3 HIS B 120 NE2 89.4 120.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 63 ND1
REMARK 620 2 HIS B 71 ND1 102.9
REMARK 620 3 HIS B 80 ND1 107.6 116.8
REMARK 620 4 ASP B 83 OD2 153.5 85.3 90.3
REMARK 620 5 ASP B 83 OD1 98.3 102.8 125.0 55.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 155
DBREF 1L3N A 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1L3N B 1 153 UNP P00441 SODC_HUMAN 1 153
SEQADV 1L3N ALA A 6 UNP P00441 CYS 6 ENGINEERED MUTATION
SEQADV 1L3N SER A 111 UNP P00441 CYS 111 ENGINEERED MUTATION
SEQADV 1L3N ALA B 6 UNP P00441 CYS 6 ENGINEERED MUTATION
SEQADV 1L3N SER B 111 UNP P00441 CYS 111 ENGINEERED MUTATION
SEQRES 1 A 153 ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 A 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 A 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 A 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 A 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 A 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 A 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 A 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 A 153 SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU
SEQRES 10 A 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 A 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 A 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 B 153 ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 B 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 B 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 B 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 B 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 B 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 B 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 B 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 B 153 SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU
SEQRES 10 B 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 B 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 B 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
HET CU1 A 154 1
HET ZN A 155 1
HET CU1 B 154 1
HET ZN B 155 1
HETNAM CU1 COPPER (I) ION
HETNAM ZN ZINC ION
FORMUL 3 CU1 2(CU 1+)
FORMUL 4 ZN 2(ZN 2+)
HELIX 1 1 GLU A 132 LYS A 136 5 5
HELIX 2 2 ASN B 131 THR B 137 1 7
SHEET 1 A 4 LYS A 3 LYS A 9 0
SHEET 2 A 4 GLN A 15 GLN A 22 -1 O ILE A 18 N ALA A 6
SHEET 3 A 4 VAL A 29 ILE A 35 -1 O TRP A 32 N ASN A 19
SHEET 4 A 4 ALA A 95 VAL A 97 -1 O VAL A 97 N GLY A 33
SHEET 1 B 4 LYS A 3 LYS A 9 0
SHEET 2 B 4 GLN A 15 GLN A 22 -1 O ILE A 18 N ALA A 6
SHEET 3 B 4 VAL A 29 ILE A 35 -1 O TRP A 32 N ASN A 19
SHEET 4 B 4 GLU A 100 ASP A 101 -1 O ASP A 101 N VAL A 29
SHEET 1 C 4 ASP A 83 ALA A 89 0
SHEET 2 C 4 GLY A 41 HIS A 46 -1 N GLY A 41 O ALA A 89
SHEET 3 C 4 THR A 116 HIS A 120 -1 O VAL A 118 N HIS A 46
SHEET 4 C 4 ARG A 143 VAL A 148 -1 O ALA A 145 N VAL A 119
SHEET 1 D 5 VAL B 94 ASP B 101 0
SHEET 2 D 5 VAL B 29 LYS B 36 -1 N VAL B 29 O ASP B 101
SHEET 3 D 5 GLN B 15 GLN B 22 -1 N ASN B 19 O TRP B 32
SHEET 4 D 5 LYS B 3 LYS B 9 -1 N ALA B 4 O PHE B 20
SHEET 5 D 5 GLY B 150 ILE B 151 -1 O GLY B 150 N VAL B 5
SHEET 1 E 2 GLY B 41 HIS B 43 0
SHEET 2 E 2 VAL B 87 ALA B 89 -1 O ALA B 89 N GLY B 41
SHEET 1 F 3 PHE B 45 HIS B 48 0
SHEET 2 F 3 THR B 116 VAL B 119 -1 O THR B 116 N HIS B 48
SHEET 3 F 3 ALA B 145 VAL B 148 -1 O GLY B 147 N LEU B 117
SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.08
SSBOND 2 CYS B 57 CYS B 146 1555 1555 2.08
LINK ND1 HIS A 46 CU CU1 A 154 1555 1555 2.08
LINK NE2 HIS A 48 CU CU1 A 154 1555 1555 2.06
LINK ND1 HIS A 63 ZN ZN A 155 1555 1555 2.06
LINK ND1 HIS A 71 ZN ZN A 155 1555 1555 2.05
LINK ND1 HIS A 80 ZN ZN A 155 1555 1555 2.07
LINK OD2 ASP A 83 ZN ZN A 155 1555 1555 2.58
LINK OD1 ASP A 83 ZN ZN A 155 1555 1555 1.85
LINK NE2 HIS A 120 CU CU1 A 154 1555 1555 2.07
LINK ND1 HIS B 46 CU CU1 B 154 1555 1555 2.03
LINK NE2 HIS B 48 CU CU1 B 154 1555 1555 2.04
LINK ND1 HIS B 63 ZN ZN B 155 1555 1555 2.06
LINK ND1 HIS B 71 ZN ZN B 155 1555 1555 2.04
LINK ND1 HIS B 80 ZN ZN B 155 1555 1555 2.03
LINK OD2 ASP B 83 ZN ZN B 155 1555 1555 2.64
LINK OD1 ASP B 83 ZN ZN B 155 1555 1555 1.94
LINK NE2 HIS B 120 CU CU1 B 154 1555 1555 2.07
SITE 1 AC1 5 HIS A 46 HIS A 48 HIS A 63 VAL A 118
SITE 2 AC1 5 HIS A 120
SITE 1 AC2 5 HIS A 63 HIS A 71 HIS A 80 ASP A 83
SITE 2 AC2 5 LYS A 136
SITE 1 AC3 5 HIS B 46 HIS B 48 HIS B 63 VAL B 118
SITE 2 AC3 5 HIS B 120
SITE 1 AC4 4 HIS B 63 HIS B 71 HIS B 80 ASP B 83
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - ct 27 Bytes